ID R7SWE9_DICSQ Unreviewed; 416 AA.
AC R7SWE9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 08-NOV-2023, entry version 56.
DE SubName: Full=Protease {ECO:0000313|EMBL:EJF60406.1};
GN ORFNames=DICSQDRAFT_127694 {ECO:0000313|EMBL:EJF60406.1};
OS Dichomitus squalens (strain LYAD-421) (Western red white-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Dichomitus.
OX NCBI_TaxID=732165 {ECO:0000313|EMBL:EJF60406.1, ECO:0000313|Proteomes:UP000053319};
RN [1] {ECO:0000313|EMBL:EJF60406.1, ECO:0000313|Proteomes:UP000053319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LYAD-421 SS1 {ECO:0000313|EMBL:EJF60406.1,
RC ECO:0000313|Proteomes:UP000053319};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; JH719416; EJF60406.1; -; Genomic_DNA.
DR RefSeq; XP_007366824.1; XM_007366762.1.
DR AlphaFoldDB; R7SWE9; -.
DR GeneID; 18834405; -.
DR KEGG; dsq:DICSQDRAFT_127694; -.
DR HOGENOM; CLU_013253_1_4_1; -.
DR OMA; SCIANGW; -.
DR OrthoDB; 1537596at2759; -.
DR Proteomes; UP000053319; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF51; NAPSIN-A; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:EJF60406.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053319};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..416
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004445055"
FT DOMAIN 109..413
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 142..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 127
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 302
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 339..373
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 416 AA; 43710 MW; 5B560E0D84D8D3D7 CRC64;
MFCKAALITV ALALIASASP IVKPSSGIRI PIQKRGSLTN EDGTFNAEKV ARELVRVQNK
HRQNLINLKN NVGVKAFNKG ASIKPLATIP THVKRDGVDL TDQENDLLWT GEITIGTDDQ
KFVIDFDTGS SDLWVPSTSC DSCGSHNKYD PSTSGKKESG SFSISYGDGS TASGDPYTDT
VTVGGVKVNG QYLAAVTQES SEFQSDPSDG LLGLAFPAIS SLNHDPFFFT AVSQGTAKEG
RFGFKLASSG SELYIGGTNS DLYKGDIEYH DISSDNGFWQ IGGASVSVGG KSVADSFDTI
IDSGSTIITA PTDAAKSFWD AVDGSDVYDS SQGLYSYPCD SAPEVSFNWG GKDWAISSEN
LSLGETESGS GSCVGAISGG DLGLGDNVWL LGDTLLKNTY TVFSVDDNGV GFAELA
//